Qingtong Zhou

This study investigates the anti-Acanthamoeba effects of licorice-derived compounds, showing that isoliquiritigenin and glabridin inhibit growth through apoptosis induction and metabolic pathway modulation.

This study shows nitroxoline reduces Acanthamoeba castellanii viability, induces apoptosis, and alters gene expression related to DNA damage and stress response pathways.

This study reveals the molecular mechanism by which GLP-1(9-36) and the allosteric modulator LSN3318839 enhance GLP-1R signaling through distinct structural interactions.

The paper reports cryo-EM structures of RXFP4-Gi complexes with INSL5 and agonists, revealing a unique peptide-binding mechanism and subtype selectivity determinants.

This paper reports cryo-EM structures of small molecule GLP-1R agonists Boc5 and WB4-24, revealing a novel binding pocket and mechanism for peptidomimetic agonism.

This study reports the cryo-EM structure of the human VIP2R bound to PACAP27 and Gs, revealing a unique N-terminal helix conformation that stabilizes the ligand-receptor interface.

The paper determines the crystal structure of a constitutive active A2A receptor mutant to elucidate the molecular mechanism of mutation-induced activity.

The paper investigates how splice variants of GIPR modulate cAMP and β-arrestin signaling independently of ligand binding.

The paper identifies a splice variant of the GHRHR receptor that mediates constitutive signal bias towards β-arrestin recruitment, impacting downstream signaling pathways in prostate cancer cells.

This study determines cryo-EM structures of dual and triple agonists bound to GIPR, GLP-1R, and GCGR to elucidate their superior efficacy over monoagonists in glucose homeostasis.

The paper reports the cryo-EM structure of the human GIPR complexed with GIP and a Gs heterotrimer, revealing how GIP is recognized and activates the receptor.

The paper reports cryo-EM structures of GLP-1R with ago-allosteric modulators, revealing their mechanism of action and providing insights for therapeutic design.

The paper identifies a universal activation mechanism for class A GPCRs by analyzing high-resolution structures, linking ligand binding to G protein coupling through TM6 movement.